Liposome Reconstitution of Native or Reduced and Alkylated Transferrin Receptor

Abstract

Human placenta transferrin receptor has been encapsulated into liposomes in its native form or in the reduced and alkylated one. The binding capacity of the reconstituted reduced and alkylated receptor decreased of about 30% with respect to the native dimeric one, but the dissociation constant for human serum transferrin did not change significantly, being around 0.9 μM. Electron microscopy measurements showed that the encapsulation efficiency of reduced and alkylated receptor was 70-75% with respect to the native one.

As a first conclusion our results suggested that the disulfide bridges between the receptorial subunits did not play an important role on the interaction between transferrin and its specific membrane receptorial system and that the lesser binding capacity of the reduced and alkylated reconstituted receptor was due to the decreased encapsulation ability.